Redox-Controlled Stabilization of an Open-Shell Intermediate in a Bioinspired Enzyme Model
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Kristina Hanauer
- Christoph Foerster
- Katja Heinze
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000442492500002&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1002/ejic.201800570
- eISSN
- 1099-0682
- Externe Identifier
- Clarivate Analytics Document Solution ID: GR3LS
- ISSN
- 1434-1948
- Ausgabe der Veröffentlichung
- 31
- Zeitschrift
- EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
- Schlüsselwörter
- Ferrocenes
- Molybdenum
- Oxygen-atom transfer
- Redox chemistry
- Enzyme models
- Paginierung
- 3537 - 3547
- Datum der Veröffentlichung
- 2018
- Status
- Published
- Titel
- Redox-Controlled Stabilization of an Open-Shell Intermediate in a Bioinspired Enzyme Model
- Sub types
- Article
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:p>Bis(ferrocenyl)‐appended dioxido molybdenum(VI) complexes perform oxygen‐atom transfer (OAT) reactions similar to sulfite oxidases. Positively charged ferrocenium ions accelerate the nucleophilic attack of the substrate. The fate of the intermediate species formed after the OAT depends on the initial redox states of the iron centers. In the all‐iron(II) state of the ferrocenyl moieties, a simple OAT from the Fe<jats:sup>II</jats:sup>Fe<jats:sup>II</jats:sup>Mo<jats:sup>VI</jats:sup>O<jats:sub>2</jats:sub> unit to a PMe<jats:sub>3</jats:sub> substrate occurs yielding Fe<jats:sup>II</jats:sup>Fe<jats:sup>II</jats:sup>Mo<jats:sup>IV</jats:sup>O and OPMe<jats:sub>3</jats:sub> without participation of the iron(II) centers. In the all‐iron(III) state, the ferrocenium intermediates are susceptible to decomposition initiated by the nucleophilic substrate. However, in the mixed Fe<jats:sup>II</jats:sup>/Fe<jats:sup>III</jats:sup> state, OAT to PMe<jats:sub>3</jats:sub> is rapidly followed by an intramolecular electron transfer (IET) within the initially formed Fe<jats:sup>II</jats:sup>Fe<jats:sup>III</jats:sup>Mo<jats:sup>IV</jats:sup>O(OPMe<jats:sub>3</jats:sub>) species to give the Fe<jats:sup>II</jats:sup>Fe<jats:sup>II</jats:sup>Mo<jats:sup>V</jats:sup>O(OPMe<jats:sub>3</jats:sub>) electromer. The absence of ferrocenium species, the presence of molybdenum(V) and the coordinated OPMe<jats:sub>3</jats:sub> in the quite persistent Fe<jats:sup>II</jats:sup>Fe<jats:sup>II</jats:sup>Mo<jats:sup>V</jats:sup>O(OPMe<jats:sub>3</jats:sub>) electromer is demonstrated by EPR spectroscopy in combination with Density Functional Theory calculations. The IET‐coupled OAT reaction stabilizes this molybdenum(V) intermediate compared to the conventional molybdenum(IV) OAT reaction intermediate. This stabilization enables its characterization by spectroscopic means before the OPMe<jats:sub>3</jats:sub> product dissociates. This study presents a concept for redox‐controlled stabilization of a catalytically relevant intermediate.</jats:p>
- Autoren
- Kristina Hanauer
- Christoph Förster
- Katja Heinze
- DOI
- 10.1002/ejic.201800570
- eISSN
- 1099-0682
- ISSN
- 1434-1948
- Ausgabe der Veröffentlichung
- 31
- Zeitschrift
- European Journal of Inorganic Chemistry
- Sprache
- en
- Online publication date
- 2018
- Paginierung
- 3537 - 3547
- Datum der Veröffentlichung
- 2018
- Status
- Published
- Herausgeber
- Wiley
- Herausgeber URL
- http://dx.doi.org/10.1002/ejic.201800570
- Datum der Datenerfassung
- 2023
- Titel
- Redox‐Controlled Stabilization of an Open‐Shell Intermediate in a Bioinspired Enzyme Model
- Ausgabe der Zeitschrift
- 2018
Datenquelle: Crossref
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